• 検索結果がありません。

91

1) Castellanos JR, Prieto JM, Heinrich M. Red Lapacho (Tabebuia impetiginosa)–A global ethnopharmacological commodity? J. Ethnopharmacol. 2009;121:1–13.

2) Mowrey, D.B. Ancient Herb, Modern Medicine. Mountainwest Institute of Herbal Sciences, Salt Lake City. 2001.

3) Queiroz MLS, Valadares MC, Torello CO, Ramos AL, Oliveira AB, Rocha FD, Arruda VA, Accorci WR. Comparative studies of the effects of Tabebuia avellanedae bark extract β-lapachone on the hematopoietic response of tumor-bearing mice. J. Ethnopharmacol.

2008;117:228–235.

4) 畑中正明, 福田陽一. Tabebuia avellanedae(タヒボ)を摂取した食道癌の1例. 日本補 完代替医療学会誌. 2015;12:107–108.

5) Byeon SE, Chung JY, Lee YG, Kim BH, Kim KH, Cho JY, In vitro and in vivo anti-inflammatory effects of taheebo, a water extract from the inner bark of Tabebuia avellanedae.

J. Enthnopharmacol. 2008;119:145–152.

6) Freitas AE, Budni J, Lobato KR, Binfaré RW, Machado DG, Jacinto J, Veronezi PO, Pizzolatti MG, Rodrigues ALS. Antidepressant-like action of the ethanolic extract from Tabebuia avellanedae in mice: Evidence for the involvement of the monoaminergic system. Prog.

Neuropsychopharmcol. Biol.Psychiatry. 2010:34;335-343.

7) Park HJ, Lee SW, Kwon DJ, Heo SI, Park SH, Kim SY, Hong S. Oral administration of taheebo (Tabebuia avellanedae Lorentz ex Griseb.) water extract prevents DSS-induced colitis in mice by up-regulating type II T helper immune responses. BMC Complement. Altern. Med.

2017:17;448.

8) Iwamoto K, Fukuda Y, Tokikura C, Noda M, Yamamoto A, Yamamoto M, Yamashita M, Zaima N, Iida A, Moriyama T. The anti-obesity effect of Taheebo (Tabebuia avellanedae Lorentz ex Griseb) extract in ovariectomized mice and the identification of a potential anti-obesity compound. Biochem. Biophys. Res. Commun. 2016:478;1136–1140.

9) (a) Suffnes, M., Douros, J.D., Miscellaneous natural products with antitumor activity. In: Case study. Anticancer Agents Based on Natural Product Models. Academic Press, New York, 1980 p474. (b) Block JB, Serpick AA, Miller W, Wiernik PH, Early clinical studies with lapachol (NSC-11905) Cancer Chemother. Rep. 2. 1974;4:27-28.

10) Clinical Trials. gov NCT01502800. Clinical Trial of ARQ 761 in Advanced Solid Tumors.

11) Li CJ, Averboough L, Pardee AB. beta-Lapachone, a novel DNA topoisomerase I inhibitor with a mode of action different from camptothecin. J. Biol. Chem. 1993;268:22463-22468.

92

12) Pink J., Planchon SM, Tagliarino C, Varnes ME, Siegel D, Boothman DA, NAD(P)H:

Quinone oxidoreductase activity is the principal determinant of betalapachone cytotoxicity. J.

Biol. Chem. 2000:275;5416–5424.

13) Lim SM, Jeong Y, Lee S, Im H, Tae HS, Kim BG, Park HD, Park J, Hong S. Identification of β‑Lapachone Analogs as Novel MALT1 Inhibitors To Treat an Aggressive Subtype of Diffuse Large B‑Cell Lymphoma. J. Med. Chem. 2015;58:8491-8502.

14) (a) Yamashita M, Kaneko M, Iida A, Tokuda H, Nishimura K, Stereoselective synthesis and cytotoxicity of a cancer chemopreventive naphtoquinone from Tabebuia avellanedae. Bioorg.

Med. Chem. Lett. 2007;17:6417–6420. (b) Yamashita M, Kaneko M, Tokuda H, Nishimura K, Kumeda Y, Iida A, Synthesis and evaluation of bioactive naphtoquinones from the Brazilian medical plant, Tabebuia avellanedae. Bioorg. Med. Chem. 2009;17:6286–6291. (c) Yamashita M, Ueda K, Sakaguchi K, Tokuda H, Iida A, One-Pot Synthesis of Benzo[f]indole-4,9-diones from1,4-Naphthoquinones and Terminal Acetylenes. Chem. Pharm. Bull. 2011;59:1289–1293.

(d) Ueda K, Yamashita M, Sakaguchi K, Tokuda H, Iida A, Concise Synthesis of Heterocycle-Fused Naphthoquinones by Employing Sonogashira Coupling and Tandem Addition-Elimination/Intramolecular Cyclization. Chem. Pharm. Bull. 2013;61:648–654.

15) (a) Debnath B, Xu S, Neamati N, Small Molecule Inhibitors of Signal Transducer and Activator of Transcription 3 (Stat3) Protein. J. Med. Chem. 2012;55:6645–6668.

(b) Johnson DE, O’Keefe RA, Grandis JR. Targeting the IL-6/JAK/STAT3 signalling axis in cancer. Nat. Rev. Clin. Oncol. 2018;15:234–248.

(c) Beebe, JD, Liu J-Y, Zhang J-T. Two decades of research in discovery of anticancer drugs targeting STAT3, how close are we? Pharmacol. Ther. 2018;191:74–91.

(d) Schwartz DM, Kanno Y, Villarino A, Ward M, Gadina M, O)shea JJ. JAK inhibition as a therapeutic strategy for immune and inflammatory diseases. Nat. Rev. Drug Discov.

2017;16:843-862.

16 ) Mandal PK, Ren Z, Chen X, Xiong C, Murray JS. Structure-Affinity Relationships of Glutamine Mimics Incorporated into Phosphopeptides Targeted to the SH2 Domain of Signal Transducer and Activator of Transcription 3. J. Med. Chem. 2009;52:6126-6141.

17) Buettner R, Corzano R, Rashid R, Lin J, Senthil M, Hedvat M, Schroeder A, Mao A, Herrmann A, Yim J, Li H, Yuan Y-C, Yakusshijin K, Yakushijin F, Vaidehi N, Moore R, Gugiu G, Lee TD, Yip R, Chen Y, Jove R, Horne D, Williams JC. Alkylation of Cysteine 468 in Stat3 Defines a Novel Site for Therapeutic Development. ACS Chem. Biol. 2011;6:432-443.

18) Hahn Y-I, Kim S-J, Choi B-Y, Cho K-C, Bandu R, Kim KP, Kim D-H, Kim W, Park JS, Han BW, Lee J, Na H-K, Cha Y-N, Surh Y-J. Curcumin interacts directly with the Cysteine 259

93

residue of STAT3 and induces apoptosis in H-Ras transformed human mammary epithelial cells. Sci. Rep. 2018;9:6409-6422.

19) Li CJ, Yang A, Rogoff H. Method of Targeting Stat3 and Other Non-druggable Proteins.

WO2017023866A1.

20 ) Ren Z, Cabell LA, Schaefer TS. McMurray JS. Identification of a high-affinity phosphopeptide inhibitor of Stat3. Bioorg. Med. Chem. Lett. 2003:13;633−636.

21) Song H, Wang R, Wang S, Lin J. A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells. Proc. Natl. Acad. Sci.

2005:102;4700–4705.

22) (a) Bhasin D, Cisek K, Pandharkar T, Regan N, Li C. Pandit B, Lin J, Li PK, Design, synthesis, and studies of small molecule STAT3 inhibitors. Bioorg. Med. Chem. Lett. 2008:18;391−395.

(b) Lin L, Hutzen B, Li PK, Ball S, Zuo M, DeAngelis S, Foust E, Sobo M, Friedman L, Bhasin D, Cen L, Li C, Lin J. A novel small molecule, LLL12, inhibits STAT3 phosphorylation and activities and exhibits potent growth-suppressive activity in human cancer cells. Neoplasia 2010:12;39−50. (c) Song H, Wang R, Wang S, Lin, J. Small Molecule Inhibitors of Stat3 and the Uses Thereof. WO 2006/091837 A2, 200.

23) Brambilla L, Genini, D, Laurini E, Merulla J, Perez L, Fermeglia F, Carbone GM, Pricl S, Catapano CV. Hitting the right spot: Mechanism of action of OPB-31121, a novel and potent inhibitor of the Signal Transducer and Activator of Transcription 3 (STAT3). Mol. Oncol.

2015;9:1194–1206.

24 ) ClinicalTrials.gov. NCT01406574. Phase I/II Study of OPB-31121 in Patients With Progressive Hepatocellular Carcinoma.

25) Buettner R, Corzano R, Rashid R, Lin J, Senthil M, Hedvat M, Schroeder A, Mao A, Herrmann A, Yim J, Li H, Yuan YC, Yakusijin K, Yakushijin F, Vaidehi N, Moore R, Gugiu G, Lee TD, Yip R, Chen Y, Jove R, Horne D, Williams JC. Alkylation of Cysteine 468 in Stat3 Defines a Novel Site for Therapeutic Development. ACS Chem. Biol. 2011;6:432-443.

26) Sabanés Zariquiey F, da Souza JV, Estrada-Tejedor R, Bronowska AK. If You Cannot Win Them, Join Them: Understanding New Ways to Target STAT3 by Small Molecule. ACS Omega 2019;4:13913–13921.

27) Zhou Q, Peng C, Du F, Zhou L, Shi Y, Du Y, Liu D, Sun W, Zhang M, Chen G. Design, synthesis and activity of BBI608 derivatives targeting on stem cells. Euro. J. Med. Chem.

2018;151:39-50.

94

28) Li C, Chen C, An Q, Yang Tao, Sang Z, Yang Y, Ju Y, Tong A, Luo Y. A novel series of napacucasin derivatives as orally active inhibitors of signal transducer and activator of transcription 3 (STAT3). Euro. J. Med. Chem. 2019;162:543-554.

29) Bi S, Chen K, Feng L, Fu G, Yang Q, Deng M, Zhao H, Li Z, Fang Z, Xu B. Napabucasin (BBI608) eliminate AML cells in vitro and in vivo via inhibition of STAT3 pathway and induction of DNA damage. Euro. J. Pharm. 2019;855:252–261.

30) Clinical Trials. gov NCT 03522649. A Phase III Clinical Study of Napabucasin (GB201) Plus FOLFIRI in Adult Patients With Metastatic Colorectal Cancer.

31) Li Y, Rogoff HA, Keates S, Gao Y, Murikipudi S, Mikule K, Leggett D, Li W, Pardee AB, Li CJ. Suppression of cancer relapse and metastasis by inhibiting cancer stemness. Proc. Natl.

Acad. Sci. USA. 2015;112:1839–1844.

32) Girard M, Kindack D, Dawson BA, Ethier JC, Awang DVC, Naphthoquinone constituents of Tabebuia spp. J. Nat. Prod. 1988;51:1023-1024.

33) (a) Haan S, Hemmann U, Hassiepen U, Schaper F, Schneider-Mergener J, Wollmer A, Heinrich PC, Grötzinger J. Characterization and Binding Specificity of the Monomeric STAT3-SH2 Domain. J. Biol Chem. 1999;275:1342-1348. (b) Schust J, Berg T. A high-throughput fluorescence polarization assay for signal transducer and activator of transcription 3. Anal. Biochem. 2004;330:114-118.

34) Becker S. Groner B. Müller CW. Three-dimensional structure of the Stat3b homodimer bound to DNA. Nature 1998;394:146-151.

35 ) van de Waterbeemd H, Smith DA, Beaumont K, Walker DK. Property-Based Design:

Optimization of Drug Absorption and Pharmacokinetics. J. Med. Chem. 2001:44;1313–1333.

36) Ottaviani G, Martel S, Carrupt P.-A. Parallel Artificial Membrane Permeability Assay: A New Membrane for the Fast Prediction of Passive Human Skin Permeability. J. Med. Chem.

2006:49;3948–3954.

37) van Breemen RB, Li Y. Caco-2 cell permeability assays to measure drug absorption. Expert Opin Drug Metab Toxicol. 2005:1;175–185.

38) Senger MR, Fraga CAM, Dantas RF, Silva Jr. FP. Filtering promiscuous compounds in early drug discovery: is it a good idea? Drug Discov. Today 2016:21;868–872.

関連したドキュメント